<result><BiopanningDataSet><Item><BiopanningDataSetID>476</BiopanningDataSetID>
<Peptides>NMIESMLRTASH(1)
NPVEWFMSTVNT(1)
NPIESMLRTASH(1)</Peptides>
<Motif>NPVE</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples before rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by competition with FVIII in excess. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>477</BiopanningDataSetID>
<Peptides>NPVELLL(1)
NPVELGI(1)</Peptides>
<Motif>NPVE</Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples before rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by competition with FVIII in excess. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>478</BiopanningDataSetID>
<Peptides>NPVEALLRPLGS(1)
NPVENMMDRDSQ(1)
NPVERLLTSALA(1)
NPVEWLMSTVNT(1)</Peptides>
<Motif>NPVE</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples after rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by pH-shift using glycine-HCl, pH 2.2. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>479</BiopanningDataSetID>
<Peptides>NPVEHMM(2)
NPVENLT(1)
NPVETQV(1)</Peptides>
<Motif>NPVE</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples after rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by pH-shift using glycine-HCl, pH 2.2. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>480</BiopanningDataSetID>
<Peptides>NPIESMLRTASH(1)
NPIEQLLRASYN(1)
NPIENALGVREI(1)</Peptides>
<Motif>NPIE</Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples after rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by competition with FVIII in excess. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>481</BiopanningDataSetID>
<Peptides>NPVEHMM(1)
NPVELGI(1)
NPVEFHT(1)
NPVESLL(1)</Peptides>
<Motif>NPVE</Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (subtractive panning, competitive panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18715645</Reference>
<Target_Name>FVIII inhibitor positive plasma samples after rituximab treatment</Target_Name>
<Template_Name>Coagulation factor VIII</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The FVIII inhibitor titer of the target is 23 BUs/ml ( BU = Bethesda Unit, corresponds to 50% reduction of FVIII activity). An IgG preparation mixed 1:1 with plasma of a healthy donor was used in 2 negative selections to remove non-specific phages. For 3 rounds of positive selection, binding phages were eluted by competition with FVIII in excess. Although 300 phage clones were analyzed, only above sequences were given in the original paper.</Brief_Description>
<BiopanningDataSet_Comments>The template of these peptides might be A2 domain of factor VIII.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>482</BiopanningDataSetID>
<Peptides>MPPPLMQ
FHENWPS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17972282</Reference>
<Target_Name>Carbon Black FW-18</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>483</BiopanningDataSetID>
<Peptides>RTAPTTPLLLSL
WHLSWSPVPLPT</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17972282</Reference>
<Target_Name>Carbon Black FW-18</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>484</BiopanningDataSetID>
<Peptides>VPRVTSI
MANHNLS
FHENWPS</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17972282</Reference>
<Target_Name>Long fibrous cellulose</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-7 phage display library (X7)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Phage ELISA showed that FHENWPS did not show specific binding activity to cellulose.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>485</BiopanningDataSetID>
<Peptides>THKTSTQRLLAA
KCCYVNVGSVFS
AHMQFRTSLTPH</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:17972282</Reference>
<Target_Name>Long fibrous cellulose</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Phage ELISA showed that AHMQFRTSLTPH did not show specific binding activity to cellulose.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>486</BiopanningDataSetID>
<Peptides>WYRGRL(94)
DPHFHL(1)
RVMLVR(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18246072</Reference>
<Target_Name>Denuded cartilage grafts</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>f3-6mer phage display library (X6)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>WYRGRL was selected in 94 of 96 clones sequenced after five rounds of biopanning and was demonstrated to bind to collagen IIα1. Peptide-functionalized nanoparticles targeted articular cartilage up to 72-fold more than nanoparticles displaying a scrambled peptide sequence following intra-articular injection in the mouse.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>487</BiopanningDataSetID>
<Peptides>ATETLARSLRLF(1)
YKHGMVTVGSTP(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>2</Rounds_of_Panning>
<Reference>PMID:18952877</Reference>
<Target_Name>Magnetic particles (BacMPs)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The BacMPs obtained from Magnetospirillum magneticum strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane.</Brief_Description>
<BiopanningDataSet_Comments>Forty-six clones were randomly picked from positive phages and sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>488</BiopanningDataSetID>
<Peptides>KSLSRHDHIHHH(2)
HQTVVRPIPLFR(1)
ASHMSWLGPGLR(1)
SSLYPARLQGMS(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>4</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18952877</Reference>
<Target_Name>Magnetic particles (BacMPs)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The BacMPs obtained from Magnetospirillum magneticum strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane.</Brief_Description>
<BiopanningDataSet_Comments>Fourteen clones were randomly picked from positive phages and sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>489</BiopanningDataSetID>
<Peptides>KPQQHNRPLRHK
KIPHPEHPTKFR
VFAGKPSHKPPH</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>3</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18952877</Reference>
<Target_Name>Magnetic particles (BacMPs)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The BacMPs obtained from Magnetospirillum magneticum strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane.</Brief_Description>
<BiopanningDataSet_Comments>Twenty-four clones were randomly picked from positive phages and sequenced.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>490</BiopanningDataSetID>
<Peptides>QFNVQKVPKSKP(2)
GPVHKHLPKAHK(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18952877</Reference>
<Target_Name>Magnetic particles (BacMPs)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The BacMPs obtained from Magnetospirillum magneticum strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane.</Brief_Description>
<BiopanningDataSet_Comments>Twenty-four clones were randomly picked from positive phages and sequenced. The peptides given in the original articles were highly cationic and could bind onto the BacMP membrane. They exhibited antimicrobial activity against Bacillus subtilis but not against Escherichia coli and Saccharomyces cerevisiae.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>491</BiopanningDataSetID>
<Peptides>GPVHKHLPKAHK(3)
KPIHHHPHLPLK(2)
KPQQHNRPLRHK(2)
KIPHPEHPTKFR(2)
VFAGKPSHKPPH(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>6</Rounds_of_Panning>
<Reference>PMID:18952877</Reference>
<Target_Name>Magnetic particles (BacMPs)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The BacMPs obtained from Magnetospirillum magneticum strain AMB-1 consist of pure magnetite (50 to 100 nm in size) and are covered with a lipid bilayer membrane derived from the invagination of the inner membrane.</Brief_Description>
<BiopanningDataSet_Comments>Forty-eight clones were randomly picked from positive phages and sequenced. The peptides given in the original articles were highly cationic and could bind onto the BacMP membrane. They exhibited antimicrobial activity against Bacillus subtilis but not against Escherichia coli and Saccharomyces cerevisiae.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>492</BiopanningDataSetID>
<Peptides>ETPLTETALKWH(29)
FNGSHIYSPFHP(7)
HLQDGSPPSSPH(6)
APVPPTAWWHLS(5)
QWNLTPRQSLQL(4)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>5</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:19226949</Reference>
<Target_Name>Anti-H5N1 virus monoclonal antibody 8H5</Target_Name>
<Template_Name>Hemagglutinin</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Sixty positive clones were sequenced. ETPLTETALKWH was further displayed on the virus-like particle assembled from aa 1-149 fragment of HBcAg. The chimeric particle conserved the specific binding to 8H5 mAb, and competed with H5N1 viruses for 8H5 mAb.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>493</BiopanningDataSetID>
<Peptides>VGPRR
FLLCEQ
RVPMAR
RWPELE
PRVKGA
ADGRAV
GMVGQG
HGRKRR
GSWSSM
RARATM
LWRGPK
AVVLLS
SRGRLG
GYGVDA
VRSLIF
RDRLPP
PGSRER
QVDQGS
GRVNG
PERCWM
RCITAR</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>21</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18979633</Reference>
<Target_Name>Implantation serine proteinase complex (Serine protease 28, 29)</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X6 T7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>494</BiopanningDataSetID>
<Peptides>SRARSA(2)
LRAAFQ(1)
VLWTLR(1)
KDLLKC(1)
GGFTHV(1)
YRSVEW(1)
RTATGR(1)
KRSTVR(1)
LRRGGV(1)
VAARSA(1)
VMVRSV(1)
MTFRSA(1)
ARSIRV(1)
GESTHG(1)
VEVAKD(1)
WFDNTM(1)
QRGVLR(1)
ARRWRR(1)
RARLRQ(1)
SGWRVG(1)
RFRQKF(1)
WKRQRW(1)
NRRSWK(1)
ERSRRS(1)
GGWRKA(1)
YNRMAG(1)
YSSKRA(1)
RRRGNG(1)
LGVRAR(1)
QVTRKV(1)
ARGSRG(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>31</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18979633</Reference>
<Target_Name>Kallikrein-6</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>X6 T7 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments></BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>495</BiopanningDataSetID>
<Peptides>LDVVLAWRDGLSGAS
GVVWRYTAPVHLGDG</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>2</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18157673</Reference>
<Target_Name>Monoclonal antibody ME361</Target_Name>
<Template_Name>GD2 ganglioside</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>fUSE5-based X15 phage display library</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>The peptides inhibited binding of the mAb to GD2. When coupled to keyhole limpet hemocyanin (KLH) or presented as multiantigenic peptides in QS21 adjuvant, the peptides induced in mice antibodies binding specifically to GD2 and delayed-type hypersensitive lymphocytes reactive specifically with GD2-positive D142.34 mouse melanoma cells. The immunity elicited by the peptides significcantly inhibited growth of GD2-positive melanoma cells in mice.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>496</BiopanningDataSetID>
<Peptides>NVVRQ(2)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Bacterial display (subtractive panning)</Experimental_Method>
<Rounds_of_Panning>4</Rounds_of_Panning>
<Reference>PMID:18765541</Reference>
<Target_Name>Highly metastatic prostate carcinoma cell line PC-3M-1E8</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>FliTrx bacterial display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>The peptides were selected in vitro by screening of the FliTrx library with the highly metastatic prostate carcinoma cell line PC-3M-1E8 for four rounds. For each round, 1e8 FliTrx cells were added to a cell culture dish with the non-metastatic human prostate cancer cell line, PC-3M-2B4, for negative selection, and then incubated for 1 h with PC-3M-1E8 cells for positive selection. </Brief_Description>
<BiopanningDataSet_Comments>After four rounds, 100 individual FliTrx clones were selected and their peptide-encoding inserts were sequenced and analyzed for potential repetitive peptide motifs. However, only one sequence NVVRQ was given in the original paper. NVVRQ-displaying FliTrx clone 27 or 50 specifically bound to PC-3M-1E8 cells 12.6 or 11.7 times over control PC-3M-2B4 cells, respectively. NVVRQ specifically bound to a series of highly metastatic tumor cells, including prostate cancer PC-3M-1E8, breast cancer MDA-MB-435S, lung cancer PG-BE1, and gastric cancer MKN-45sci, in vitro and in vivo but not to the poorly metastatic or non-metastatic cell line, including prostate cancer PC-3M-2B4, breast cancer MCF-7, lung cancer PG-LH7, or murine fibroblast cell NIH/3T3. FITC-NVVRQ strongly and specifically targeted the metastasis foci in tumor-bearing mice 24 h after i.v. peptide injection.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>497</BiopanningDataSetID>
<Peptides>CHAQGSAEC(11)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18978306</Reference>
<Target_Name>Mouse thymus vasculature</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Eleven clones were sequenced. All of them has the same sequence CHAQGSAE.Immunohistochemistry confirmed that the phage peptide CHAQGSAEC can bind specifically to thymus blood vessels in mice. Furthermore, phage peptide CHAQGSAEC and free peptide CHAQGSAEC can inhibit the bioactivity of thymus output in vivo.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>498</BiopanningDataSetID>
<Peptides>CEMQTSTAC(1)
CHSSPTLYC(1)
CQSEVSQLC(1)
CPLITAAFC(1)
CLGNKAHTC(1)
CNKGAGKYC(1)
CSPDLPQRC(1)
CGTNKPWNC(1)
CMPNTLREC(1)
CTPRADRHC(1)
CTQHNPHQC(1)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>11</Unique_Sequence_Number>
<Experimental_Method>Phage display (in vivo)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18978306</Reference>
<Target_Name>Mouse kidney</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-C7C phage display library (CX7C)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>Eleven clones were sequenced. </BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>499</BiopanningDataSetID>
<Peptides>NSLSNASEFRAP(6)</Peptides>
<Motif></Motif>
<Unique_Sequence_Number>1</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>5</Rounds_of_Panning>
<Reference>PMID:18330476</Reference>
<Target_Name>Angiopoietin-1 receptor</Target_Name>
<Template_Name>Angiopoietin-1, ANG-1</Template_Name>
<Structure_of_Target_Template_Complex>4K0V ,</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description>Phages bound to Tie2 receptors were eluted with angiopoietin-2.</Brief_Description>
<BiopanningDataSet_Comments>After five rounds of screening, 20 phage clones were picked out randomly and amplified for DNA sequencing. Of these, only 17 clones had efficiently inserted peptides, and approximately 35% (6/17) of recovered clones expressed the consensus amino acid sequence NSLSNASEFRAP. Binding assays and Scatchard analysis revealed that NSLSNASEFRAP could specifically bind to Tie2 with a dissociation constant of 2.1×10−8 M. In addition, it wa showed that NSLSNASEFRAP was internalized into tumor cells highly expressing Tie2. Another enriched phage clone displayed a peptide XXGTHGHCQLSH, which did not have binding specificity for Tie2.</BiopanningDataSet_Comments>
</Item><Item><BiopanningDataSetID>500</BiopanningDataSetID>
<Peptides>QMDTSTSLAPSR(1)
VPFTLQTRSLSD(1)
TVTPSNISFTPS(1)
ASTLINPLSISL(1)
AGSTASVTPAKH(1)
QMANSVMPLSWT(1)
YAHSHDKYHPN(1)
NQSPHSTYTLKP(1)
HNYPQSYRPPIV(1)
TDNNTTALTPSH(1)
TMNNTTATVSPS(1)
FQKQTNQSVSVS(1)
VHMTPTNLTPNL(1)
TFSYHNSNSPT(1)
VPDHQVSYTLSR(1)
IFHSHASLSPNS(1)
ADNANVSTLHPT(1)
VNQQPSSAFSPS(1)
LSTVQTISPSNH(1)
DMNHTKSSYNPS(1)</Peptides>
<Motif>[ST]-[AVLIFYWFYW]-[ST]-P-[ST]</Motif>
<Unique_Sequence_Number>20</Unique_Sequence_Number>
<Experimental_Method>Phage display (common panning)</Experimental_Method>
<Rounds_of_Panning>3</Rounds_of_Panning>
<Reference>PMID:18546729</Reference>
<Target_Name>Hematite particles</Target_Name>
<Template_Name>Not determined.</Template_Name>
<Structure_of_Target_Template_Complex>Not determined.</Structure_of_Target_Template_Complex>
<Structure_of_Target_Peptide_Complex>Not determined.</Structure_of_Target_Peptide_Complex>
<Library_Name>Ph.D.-12 phage display library (X12)</Library_Name>
<Affinity_Measurement_Method></Affinity_Measurement_Method>
<Affinity_Measurement_Description></Affinity_Measurement_Description>
<Brief_Description></Brief_Description>
<BiopanningDataSet_Comments>A search of published sequence data revealed that the binding motif (Ser/Thr-Pro-Ser/Thr) is adjacent to the terminal heme-binding domain of both OmcA and MtrC, which are outer membrane cytochromes from the metal reducing bacterium Shewanella oneidensis MR-1. The entire five amino acid consensus sequence (Ser/Thr-hydrophobic/aromatic-Ser/Thr-Pro-Ser/Thr) was also found as multiple copies in the primary sequences of metal-oxide binding proteins Sil1 and Sil2 from Thalassiosira pseudonana. It is suggested that this motif constitutes a natural metal-oxide binding archetype that could be exploited in enzyme-based biofuel cell design and approaches to synthesize tailored metal-oxide nanostructures.</BiopanningDataSet_Comments>
</Item></BiopanningDataSet></result>